NMR Studies on the N-Terminal Acetylation Domain of Histone H4

Bulletin of the Korean chemical society

Weontae Lee¹  Dai Woon Lee¹  Jong-Bok Yoon¹  Joohee Chung¹  Chang-Hun Lee¹  Eunjung Bang¹ 

关键词: Histone H4;    Acetylation;    NMR structure.;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

Histones, nuclear proteins that interact with DNA to form nucleosomes, are essential for both the regulation of transcription and the packaging of DNA within chromosomes. The N-terminal domain of histone H4 which contains four acetylation sites at lysines, may play a separate role in chromatin structure from the remainder of the H4 chain. NMR data suggest that H4NTP peptide does have relating disordered structure at physiological pH, however, it has a defined structure at lower pH conditions. The solution structure calculated from NMR data shows a well structured region comprising residues of Val21-Asp24. In addition, our results suggest that the H4NTP prefers an extended backbone conformation at acetylation sites, however, it (especially Lys 12 ) became more defined structures after acetylation for its optimum function.

【 授权许可】

Unknown